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Database: UniProt
Entry: A0A2U2HPM3_9BURK
LinkDB: A0A2U2HPM3_9BURK
Original site: A0A2U2HPM3_9BURK 
ID   A0A2U2HPM3_9BURK        Unreviewed;       343 AA.
AC   A0A2U2HPM3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Murein L,D-transpeptidase {ECO:0000313|EMBL:PWF49385.1};
GN   ORFNames=C7C56_006915 {ECO:0000313|EMBL:PWF49385.1};
OS   Massilia glaciei.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1524097 {ECO:0000313|EMBL:PWF49385.1, ECO:0000313|Proteomes:UP000241421};
RN   [1] {ECO:0000313|EMBL:PWF49385.1, ECO:0000313|Proteomes:UP000241421}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B448-2 {ECO:0000313|EMBL:PWF49385.1,
RC   ECO:0000313|Proteomes:UP000241421};
RA   Wang H.;
RT   "Massilia violaceinigra sp. nov., a novel purple-pigmented bacterium
RT   isolated from Tianshan glacier, Xinjiang, China.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SIMILARITY: Belongs to the YkuD family.
CC       {ECO:0000256|ARBA:ARBA00005992}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWF49385.1}.
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DR   EMBL; PXWF02000092; PWF49385.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U2HPM3; -.
DR   OrthoDB; 9787225at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000241421; Unassembled WGS sequence.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProt.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd16913; YkuD_like; 1.
DR   Gene3D; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR   Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR   InterPro; IPR005490; LD_TPept_cat_dom.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   InterPro; IPR038063; Transpep_catalytic_dom.
DR   PANTHER; PTHR30582:SF30; BLR4375 PROTEIN; 1.
DR   PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR   Pfam; PF01471; PG_binding_1; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR   SUPFAM; SSF47090; PGBD-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000241421};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          66..120
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
FT   DOMAIN          210..339
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   343 AA;  35249 MW;  59A4FCF27360CEDC CRC64;
     MAQPPAAAPA PGDTAATTAA TAATTTTTTS TTPKAAKNAK AAVTLDAATV NAPGAPAVAP
     ARADAASVLR AQILLNRARF SSGEIDAAFG SNVRQALSGY QRKMGLPATG VADAATWAAL
     NAGAAAALVT YTITDADVAG PFVAIPQKMA DKAKLSALGY SSVEEALGEK FHASPALLQR
     LNPGKNFSRA GEQIIVPNVL DTEPLPKASQ IVVDKTDRTL TLMDGDGKPM AQFPVTTGSK
     HDPLPLGKWK VNGISKAPVF HYNPALFWDA TAGDKKAKIP AGPNNPVGVA WVDLSKPHYG
     IHGTPVPASI GKTESHGCIR MTNWDVTTMM QSVGSGTAVL LKE
//
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